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The Measles virus surface glycoproteins, specifically the Hemagglutinin (H) and Fusion (F) proteins, are critical components of the Measles virus (MeV) virion responsible for host cell entry (StatPearls, 2023). The H protein mediates attachment by binding to cellular receptors such as signaling lymphocytic activation molecule (SLAM/CD150) and Nectin-4, while the F protein facilitates the fusion of the viral envelope with the host cell membrane (UniProt, P08362). These proteins are the primary targets for neutralizing antibodies elicited by vaccination and are the focus of antiviral development aimed at blocking viral entry (PubMed, PMC4104446). Measles remains a significant global health threat, causing severe respiratory illness, immunosuppression, and rare but fatal neurological complications like subacute sclerosing panencephalitis (CDC, 2020). Therapeutic strategies targeting these glycoproteins include live-attenuated vaccines, which provide long-term immunity, and experimental small-molecule inhibitors like ERDRP-0519 designed to disrupt the H-F protein complex (Nature Communications, 2016).
Neutralization of viral entry by blocking hemagglutinin-mediated attachment to host receptors (CD150/Nectin-4) and inhibiting fusion protein-mediated membrane fusion.
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